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Blocking the apolipoprotein E/amyloid-β interaction as a potential therapeutic approach for Alzheimer's disease
Open accessAbstract
The amyloid-β (Aβ) cascade hypothesis of Alzheimer's disease (AD) maintains that accumulation of Aβ peptide constitutes a critical event in the early disease pathogenesis. The direct binding between Aβ and apolipoprotein E (apoE) is an important factor implicated in both Aβ clearance and its deposition in the brain's parenchyma and the walls of meningoencephalic vessels as cerebral amyloid angiopathy. With the aim of testing the effect of blocking the apoE/Aβ interaction in vivo as a potential novel therapeutic target for AD pharmacotherapy, we have developed Aβ12-28P, which is a blood-brain-barrier-permeable nontoxic, and nonfibrillogenic synthetic peptide homologous to the apoE binding site on the full-length Aβ. Aβ12-28P binds with high affinity to apoE, preventing its binding to Aβ, but has no direct effect on Aβ aggregation. Aβ12-28P shows a strong pharmacological effect in vivo . Its systemic administration resulted in a significant reduction of Aβ plaques and cerebral amyloid angiopathy burden and a reduction of the total brain level of Aβ in two AD transgenic mice models. The treatment did not affect the levels of soluble Aβ fraction or Aβ oligomers, indicating that inhibition of the apoE/Aβ interaction in vivo has a net effect of increasing Aβ clearance over deposition and at the same time does not create conditions favoring formation of toxic oligomers. Furthermore, behavioral studies demonstrated that treatment with Aβ12-28P prevents a memory deficit in transgenic animals. These findings provide evidence of another therapeutic approach for AD.
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“We have used Ab12-28P in the past to successfully reduce Ab plaques load and CAA in APP SW and APP SW /PS1 M146L AD model mice.22”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [22]
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“One study found that antagonizing the apoE/Aβ interaction with a small peptide decreased Aβ pathology in the mouse brain”
From Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance (2011) · cites this paper as [57]
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In the citing paper
“A similar strategy preventing the interaction between apoE and Aβ has already been successfully used to attenuate Aβ toxicity and amyloid deposition (Sadowski et al., 2006).”
From Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis (2012) · cites this paper as Sadowski et al., 2006
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In the citing paper
“Aβ12-28P inhibits apoE4/Aβ binding with KI = 12.9 nM and neutralizes the promoting effect of apoE on Aβ fibrillization in vitro, but has no effect on self-assembly of Aβ in the absence of apoE [15].”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [15]
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“Consistently with our previously published observations [15] these results indicate that Aβ12-28P exerts an effect on serum cholesterol metabolism in addition to targeting the apoE/Aβ interaction in the brain.”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [15]
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“There is compelling evidence showing that apoE affects A accumulation by modulating both A aggregation (Ma et al., 1994;Wisniewski et al., 1994) and clearance (Sadowski et al., 2006;Deane et al., 2008;Jiang et al., 2008;Castellano et al., 2011)”
From Anti-ApoE Antibody Given after Plaque Onset Decreases Aβ Accumulation and Improves Brain Function in a Mouse Model of Aβ Amyloidosis (2014) · cites this paper as Sadowski et al., 2006
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In the citing paper
“Conversely, blocking the interaction between apoE and A (Sadowski et al., 2006) and decreasing the apoE level by overexpressing low-density lipoprotein receptor (Kim et al., 2009) or haploinsufficiency of apoE (Bales et al., 1999;Holtzman et al., 2000;Kim et al., 2011;Bien-Ly et al., 2012) results in decreased amyloidosis.”
From Anti-ApoE Antibody Given after Plaque Onset Decreases Aβ Accumulation and Improves Brain Function in a Mouse Model of Aβ Amyloidosis (2014) · cites this paper as Sadowski et al., 2006
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In the citing paper
“As we have previously shown, Ab12-28P inhibits ApoE4/Ab binding with K I Z 12.9 nmol/L, neutralizes the promoting effect of ApoE on Ab fibrillization in vitro, and reduces the load of Ab plaques and CAA when systemically administered to APP SW Tg mice.22”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [22]
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“As we have previously shown, Ab12-28P inhibits ApoE4/Ab binding with K I Z 12.9 nmol/L, neutralizes the promoting effect of ApoE on Ab fibrillization in vitro, and reduces the load of Ab plaques and CAA when systemically administered to APP SW Tg mice.22”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [22]
The cited source says what the claim attributes to it.
In the citing paper
“As we have previously shown, Ab12-28P inhibits ApoE4/Ab binding with K I Z 12.9 nmol/L, neutralizes the promoting effect of ApoE on Ab fibrillization in vitro, and reduces the load of Ab plaques and CAA when systemically administered to APP SW Tg mice.22”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [22]
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“As apoE co-deposits with Aβ in the amyloid plaques (13–15), we examined and found that the degree of co-localization between apoE and Aβ deposition appeared to decrease in the brains carrying APOE3-Jac variant compared to those from APOE3 (Fig. S1C–F).”
From APOE3 -Jacksonville (V236E) variant reduces self-aggregation and risk of dementia (2021) · cites this paper as [14]
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Metadata
- Authors
- Sadowski, M. J., Pankiewicz, J., Scholtzova, H., Mehta, P. D., Prelli, F., Quartermain, D., & Wisniewski, T.
- Affiliations
- *Departments of Neurology,
- New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-12-05
- Volume
- 103
- Issue
- 49
- Pages
- 18787-18792
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1654132
- OpenAlex
- W2004069543
- Cited by
- 167
- References
- 29
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 3 · 2021: 7 · 2020: 8 · 2019: 8 · 2018: 6 · 2017: 7 · 2016: 5 · 2015: 5 · 2014: 16 · 2013: 13 · 2012: 16
- FWCI
- 8.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG15408, R01AG015408, AG 20747, P30AG008051, R01AG020245, K08AG020747)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta, apolipoprotein E, synthetic peptides, amyloid-beta clearance, cerebral amyloid angiopathy, amyloid plaques, amyloid-beta oligomers, memory impairment, transgenic mouse model, blood-brain barrier permeability, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Apolipoproteins E, Binding, Competitive, Female, Mice, Transgenic, Peptide Fragments, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Mice
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